Steady state and time-resolved IR spectroscopy of the native and unfolded states of bovine ubiquitin: Protein stability and temperature-jump kinetic measurements of protein folding at low pH

  • Colley C
  • Clark I
  • Griffiths-Jones S
 et al. 
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Infrared spectroscopy has been used to characterise the folded and unfolded states of bovine ubiquitin (a small protein of 76 residues) under acidic conditions (pH 1); fast time-resolved measurements of protein unfolding, initiated by a laser-induced temperature-jump of 8 °C, shows rapid refolding and β-sheet secondary structure formation on a timescale of a few milliseconds.

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